Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Reprogrammed glucose metabolism is one of the hallmarks of cancer, and increased expression of key glycolytic enzymes, such as pyruvate kinase M2 (PKM2) and lactate dehydrogenase A (LDHA), has been associated with poor prognosis in various malignancies.
|
31527446 |
2019 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
Lactate dehydrogenase A (LDHA) is an important enzyme responsible for cancer growth and energy metabolism in various cancers via the aerobic glycolytic pathway.
|
31324019 |
2019 |
Primary malignant neoplasm
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Clinical, translational and experimental data supporting the uniqueness of the LDHA gene and its product LDH5 isoenzyme are summarized and future directions for a metabolic treatment of cancer are highlighted.
|
29913092 |
2019 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
Targeting the Warburg effect via LDHA inhibition engages ATF4 signaling for cancer cell survival.
|
30209241 |
2018 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
To elucidate its role in tumor growth, we disrupted both the <i>LDHA</i> and <i>LDHB</i> genes in two cancer cell lines (human colon adenocarcinoma and murine melanoma cells).
|
30158244 |
2018 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
HK2 expression levels were increased in cancer compared with normal tissue (75.4% vs. 40%; P<0.001), however PKM2 (P=0.243) and LDHA (P=0.067) expression levels were not.
|
29552193 |
2018 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
What we discussed gives a precise insight into LDHA especially in cancer research, which will contribute to exploring cancer pathogenesis and its handling measures.
|
30403008 |
2018 |
Primary malignant neoplasm
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Warburg effect is characterized by the upregulation of HIF-1 and c-Myc regulated LDH-A, even aerobically owing to hypoxic environment and alterations in oncogenes or tumor suppressor genes in cancer.
|
29866021 |
2018 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Moreover, the relationship between CRC cells and the tumor acidic microenvironment, especially for regulating lactate production and lactate dehydrogenase A levels, is also discussed, as well as comprehensively defining different aspects of glycolytic pathways that affect cancer cell proliferation, invasion, and migration.
|
30069931 |
2018 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
The cancer associated LDHA isoform was inhibited with IC<sub>50</sub> = 117-174 µM.
|
29199484 |
2018 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
Human lactate dehydrogenase A (LDHA) has been identified as a potential therapeutic target in the area of cancer metabolism.
|
30108883 |
2017 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
Recently, several reports showed that silencing or inhibition of LDHA could suppress metastasis of human cancer including renal cell carcinoma (RCC).However, the mechanism remains unknown.
|
28983605 |
2017 |
Primary malignant neoplasm
|
0.100 |
GeneticVariation
|
group |
BEFREE |
Inhibition of LDH activity by small hairpin ribonucleic acid or expression of phospho-deficient LDHA Y10F sensitized the cancer cells to anoikis induction and resulted in attenuated cell invasion and elevated reactive oxygen species, whereas such phenotypes were reversed by its product lactate or antioxidant N-acetylcysteine, suggesting that Y10 phosphorylation-mediated LDHA activity promotes cancer cell invasion and anoikis resistance through redox homeostasis.
|
28218905 |
2017 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
Our results suggest that expressions of LDH-A and lactate by macrophage in the tumor microenvironment are major drivers of T-cell immunosuppression, strongly supporting the concept of targeting stromal LDH-A as an effective strategy to blunt tumoral immune escape.<i>Cancer Res; 77(13); 3632-43.©2017 AACR</i>.
|
28446465 |
2017 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
A number of interesting observations are made through our analyses, including (i) all nine primary cancer types show similar association patterns between stresses and LDHA, namely the strengths of the associations increase from early- to intermediate-stage cancer tissues but then make a substantial down turn at the most advanced stage; (ii) while the detailed stress types associated with LDHA may vary across different cancer types, stresses induced by apoptosis and adaptive immune responses are present universally, suggesting that these two stresses are possibly two key drivers to keep the high-level production of lactates; and (iii) there is a clear distinction between stress types associated with LDHA in precancerous tissues vs. cancer and metastasis tissues.
|
26003569 |
2015 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
Our results are validated by examining LDHA expression, at the mRNA level, in the independent data set of clear cell renal cell carcinoma cases from The Cancer Genome Atlas databases which also shows that higher lactate dehydrogenase A expression is associated with significantly shorter overall survival.
|
24885701 |
2014 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
To our knowledge, this is the first demonstration of downregulation of LDHA in cancer.
|
24366912 |
2014 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
LDH-A, the enzyme responsible for transforming pyruvate into lactate, has been demonstrated to be up-regulated in many types of cancer and to give rise to more aggressive behavior by regulating proliferation and anti-apoptosis.
|
24608789 |
2014 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
We report that LDH-A was overexpressed in 52 of 54 (96%) paraffin-embedded cancer tissue samples and 0 of 54 para-carcinoma tissue samples.
|
24679073 |
2014 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
FOXM1 and LDHA were overexpressed concomitantly in pancreatic tumors and cancer cell lines.
|
24634381 |
2014 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
Using the cancer cell line MDA-MB-435 it is shown that shRNA mediated knockdown of lactate dehydrogenase A (LDHA), a key mediator of aerobic glycolysis, results in elevated mitochondrial ROS production and a concomitant decrease in cell proliferation and motility.
|
23583676 |
2013 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
Elevated transcription by c-Myc or HIF1α may contribute to increased LDH-A in some cancer types.
|
23523103 |
2013 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
The preclinical study thus suggests that the potential medicinal application of SS for inhibiting cancer LDH-A activity and the possibility to consider epigallocatechin as a lead compound to develop LDH-A inhibitors.
|
23457597 |
2013 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
LDH-A reduction resulted in an inhibited cancer cell proliferation, elevated intracellular oxidative stress, and induction of mitochondrial pathway apoptosis.
|
21452021 |
2012 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
However, how oncogenic signals activate LDH-A to regulate cancer cell metabolism remains unclear.
|
21969607 |
2011 |